文摘
The binding of zonisamide to purified, recombinant monoamine oxidases (MAOs) has been investigated. It is a competitive inhibitor of human MAO B (Ki = 3.1 卤 0.3 渭M), of rat MAO B (Ki = 2.9 卤 0.5 渭M), and of zebrafish MAO (Ki = 30.8 卤 5.3 渭M). No inhibition is observed with purified human or rat MAO A. The 1.8 脜 structure of the MAO B complex demonstrates that it binds within the substrate cavity.